ID A0A1D6Q7R1_MAIZE Unreviewed; 662 AA.
AC A0A1D6Q7R1;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=DNA topoisomerase 2 {ECO:0000313|EMBL:AQK54503.1};
GN ORFNames=ZEAMMB73_Zm00001d051542 {ECO:0000313|EMBL:AQK54503.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:AQK54503.1};
RN [1] {ECO:0000313|EMBL:AQK54503.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Seedling {ECO:0000313|EMBL:AQK54503.1};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the type II topoisomerase family.
CC {ECO:0000256|ARBA:ARBA00011080}.
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DR EMBL; CM000780; AQK54503.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D6Q7R1; -.
DR ExpressionAtlas; A0A1D6Q7R1; baseline and differential.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:InterPro.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR Gene3D; 3.30.1360.40; -; 1.
DR Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1.
DR Gene3D; 1.10.268.10; Topoisomerase, domain 3; 1.
DR InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR InterPro; IPR013758; Topo_IIA_A/C_ab.
DR InterPro; IPR013757; Topo_IIA_A_a_sf.
DR InterPro; IPR002205; Topo_IIA_dom_A.
DR InterPro; IPR001154; TopoII_euk.
DR PANTHER; PTHR10169:SF38; DNA TOPOISOMERASE 2; 1.
DR PANTHER; PTHR10169; DNA TOPOISOMERASE/GYRASE; 1.
DR Pfam; PF00521; DNA_topoisoIV; 1.
DR PRINTS; PR01158; TOPISMRASEII.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000313|EMBL:AQK54503.1}.
FT DOMAIN 1..337
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 260..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..287
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..451
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..662
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 662 AA; 73626 MW; 9B55A09F69F0F944 CRC64;
MTSPLFLRYM PILPMVLVNG SEGIGTGWST YIPNYNPRDI LANLRRLLNG ESTVPMHPWY
RGFKGSIEKT VNTKVAGSTY TVTGIIEVLD NTTLRITELP IRRWTQDYKD YLESLAPDTK
NKDKVPFIED VTCQGDNEDV YIQFTLSEKN MNIAMEEGLV KKFKLTTTIG TSNMHLFDSD
GKIRKYDTPE QILEEFCHLR LEFYCKRKEA LLKSIKLDLK KLENKVRFIR CVVDNEIIVN
NRKRADLFLE LRQKNFDPFP KKKKRAEPAA VGALEEEENE ESPEAAGAEP SDYEYLLSMS
IGTLTLEKIQ ELNAEKQKLV DDVEELENMS PKSLWLKDLD AFEKELDVLD QMDLAEELQR
EKRINAGKKG GSKAAPKKPR KKAASKKLDS DTEDDDFEPA VAKRGAQPKK TSSKANDSAS
EDGDYVAAEN QKKQSKKASA HVDEEVDMPS LKDRLAAFNI SDSSPDHSAM ETEVTELTEQ
QNENKATEGA SKRGGRKKAS SSLATIPSDV DEEVLEVQAQ KKGRGRKPAA VVKPKAPAAA
RKRAPAQGKV TQKKIDEMLK ATEDNNTSAS SPEKKVRKMR SSPFNKKSGS ILQRGSTASA
SSGTTVEASP PSGSSAEPVG AAQPRRTARA TKKPIYISDS DPEDEVELID DSDFDADGDS
DE
//
